ALP2_ASPFC
ID ALP2_ASPFC Reviewed; 495 AA.
AC B0Y473;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Alkaline protease 2;
DE Short=ALP2;
DE EC=3.4.21.63;
DE AltName: Full=Autophagic serine protease alp2;
DE AltName: Allergen=Asp f 18;
DE Flags: Precursor;
GN Name=alp2; ORFNames=AFUB_056750;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Alkaline protease that allows assimilation of proteinaceous
CC substrates. Acts as a significant virulence factor in invasive
CC aspergillosis. Required for regular sporulation (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-
CC OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.63;
CC -!- ALLERGEN: Acts as a major allergen in patients suffering from extrinsic
CC bronchial asthma. Binds to IgE. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; DS499597; EDP51664.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y473; -.
DR SMR; B0Y473; -.
DR Allergome; 70; Asp f 18.
DR PRIDE; B0Y473; -.
DR EnsemblFungi; EDP51664; EDP51664; AFUB_056750.
DR VEuPathDB; FungiDB:AFUB_056750; -.
DR HOGENOM; CLU_011263_1_4_1; -.
DR PhylomeDB; B0Y473; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblFungi.
DR GO; GO:0000425; P:pexophagy; IEA:EnsemblFungi.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IEA:EnsemblFungi.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Allergen; Glycoprotein; Hydrolase; Protease; Serine protease; Signal;
KW Sporulation; Virulence; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..136
FT /evidence="ECO:0000250"
FT /id="PRO_0000412302"
FT CHAIN 137..495
FT /note="Alkaline protease 2"
FT /id="PRO_0000412303"
FT DOMAIN 43..136
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 146..452
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 380
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 52640 MW; A358FE8D6EE533D2 CRC64;
MKGYLSLSIL PLLVAASPVV VDSIHNGAAP ILSSMNAKEV PDSYIVVFKK HVNAESAAAH
HSWVQDIHSA QNERVELRKR SLFGFGEEAY LGLKNTFDIA GSLVGYSGHF HEDVIEQVRK
HPDVEYIEKD SEVHTMEDPT VEKSAPWGLA RISHRDSLSF GTFNKYLYAS EGGEGVDAYT
IDTGINVDHV DFEGRAQWGK TIPTDDEDAD GNGHGTHCSG TIAGRKYGVA KKANLYAVKV
LRSSGSGTMS DVVAGVEWAV KSHLKKVKDA KDGKIKGFKG SVANMSLGGG KSRTLEAAVN
AGVEAGLHFA VAAGNDNADA CNYSPAAAEN PITVGASTLQ DERAYFSNYG KCTDIFAPGL
NILSTWIGSK HAVNTISGTS MASPHIAGLL AYFVSLQPSK DSAFAVDELT PKKLKKDIIA
IATQGALTDI PSDTPNLLAW NGGGSSNYTD IIASGGYKVN ASVKDRFEGL VHKAEKLLTE
ELGAIYSEIH DAAVA
